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inactivation of both exosc9, which encodes a component of the RNA exosome, and ptbp1, which encodes an RNA-binding protein abundant in Xenopus embryonic skin, impairs embryonic Xenopus skin development.
Polypyrimidine tract binding protein prevents activity of an intronic regulatory element that promotes usage of a composite 3'-terminal exon
These results demonstrate that during early stages of splicing, exon RNP (show RNPC3 ELISA Kits) complexes are highly dynamic with many proteins failing to bind during PTBP1 arrest.
Studied interactions of polypyrimidine tract-binding protein (PTBP1), pyruvate kinase M2 (PKM2), and STAT3 (signal transducer and activator of transcription 3 (show STAT3 ELISA Kits)) in oncogenesis of anaplastic large cell lymphoma (ALCL). Results show that in ALCL cells, PTBP1 is crucial for PKM2 phosphorylation of STAT3 (show STAT3 ELISA Kits) in the nucleus.
Expression of ATG10 negatively regulated by PTBP1 and is associated with metastasis of colorectal cancer cells.
Polypyrimidine tract binding protein (PTBP1) is a heterogeneous nuclear ribonucleoprotein (hnRNP) that plays roles in most stages of the life-cycle of pre-mRNA and mRNAs in the nucleus and cytoplasm.
follow-up molecular analyses of one splicing factor (show SLU7 ELISA Kits) PTBP1 revealed its impact on disease-associated splicing patterns in Huntington's disease (HD). Collectively, our data provide genomic evidence for widespread splicing dysregulation in HD brains, and suggest the role of aberrant alternative splicing in the pathogenesis of HD
CD5 (show CD5 ELISA Kits) transcription is increased, leading to the production of three mRNA isoforms by APA (show ENPEP ELISA Kits), all contributing for protein production, at different levels. PTBP1 binds in the vicinity of pA1 (show PAGR1 ELISA Kits), leading to an increase in mRNA levels and miR (show MLXIP ELISA Kits)-204 targets the longer CD5 (show CD5 ELISA Kits) mRNA.
Increased expression of microRNA miR (show MLXIP ELISA Kits)-145 combined with knockdown of PTBP1 protein contributed to the greater and longer growth suppression compared with each single treatment.
MiR-133b switched the PKM isoform expression from PKM2 to PKM1 through the silencing of PTBP1, which is an alternative splicer of PKM, leading to growth suppression through the induction of autophagy in part by the metabolic switching from glycolysis to oxidative phosphorylation for a short period of time.
Results suggested that PTBP1 and PTBP1-associated miR-1 and -133b are crucial molecules for the maintenance of the Warburg effect in colorectal tumors.
The polypyrimidine tract binding protein 1 (PTBP1) shields specific retroviral and cellular transcripts from nonsense-mediated mRNA decay.
Results indicate that heterogeneous nuclear ribonucleoprotein I (hnRNPI) plays a critical role in establishing neonatal immune adaptation and preventing colitis and colorectal cancer.
Thus, PTBP1 controls the activity of Pbx1 (show PBX1 ELISA Kits) to suppress its neuronal transcriptional program prior to induction of neuronal progenitor cells development.
showed polypyrimidine tract binding protein (PTBP)-dependent alternative splicing of CaMKIIalpha (show CAMK2 ELISA Kits) transcripts in the lens
This may account for the tight correlation between Hps1 with Ptbp1 expression levels observed across mammalian tissues.
The expression levels of three splicing factors, ESRP1 (show ESRP1 ELISA Kits), PTB and SF2/ASF (show SRSF1 ELISA Kits), are significantly altered during cardiac hypertrophy in mice.
Study reports that repression of a single RNA binding polypyrimidine-tract-binding (PTB) protein, which occurs during normal brain development via the action of miR (show MLXIP ELISA Kits)-124, is sufficient to induce trans-differentiation of fibroblasts into functional neurons.
The polypyrimidine tract binding proteins PTBP1 and PTBP2 (show PTBP2 ELISA Kits) repressed Psd-95 (show DLG4 ELISA Kits) (also known as Dlg4 (show DLG4 ELISA Kits)) exon 18 splicing, leading to premature translation termination and nonsense-mediated mRNA decay.
PTBP1 is not required for the earliest isovolumetric divisions and differentiation steps of the zygote up to the formation of the blastocyst.
RBM4 (show RBM4 ELISA Kits) may synergize its effect on muscle cell-specific alternative splicing by down-regulating PTB expression and antagonizing the activity of PTB in exon selection
splicing repressors hnRNP A1 and A2, as well as the polypyrimidine-tract-binding protein PTB, contribute to control of pyruvate kinase isoform M1 and M2 expression
Data report on a zebrafish maternal-effect (show NLRP5 ELISA Kits) mutant, brom bones, which is defective in the cytosolic Ca(2 (show CA2 ELISA Kits)+) rise and subsequent egg activation events, including cortical granule exocytosis and cytoplasmic segregation [brom bones].
Two stretches of polypyrimidine tracts designated PPT1 and PPT2 which influence the IRES activity of cx55.5 protein were identified; deletion of PPT1 results in an appreciable decrease of the IRES activity
PTB1 is a splicing factor (show SLU7 ELISA Kits) that influences alternative splicing and acts at the polypyrimidine tract.
Alternative splicing (AS) patterns as well as the expression of key flowering regulators were massively changed in a PTB1/2 level-dependent manner.
AtPTB1 and AtPTB2 are widely expressed in almost all tissues, with the highest expression levels in late-maturing and mature pollen grains, and are crucial for pollen germination. [AtPTB1]
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA-binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has four repeats of quasi-RNA recognition motif (RRM) domains that bind RNAs. This protein binds to the intronic polypyrimidine tracts that requires pre-mRNA splicing and acts via the protein degradation ubiquitin-proteasome pathway. It may also promote the binding of U2 snRNP to pre-mRNAs. This protein is localized in the nucleoplasm and it is also detected in the perinucleolar structure. Alternatively spliced transcript variants encoding different isoforms have been described.
polypyrimidine tract binding protein 1
, hnrnp I
, hnRNP I-related RNA transport protein VgRBP60
, polypyrimidine tract-binding protein
, polypyrimidine tract-binding protein 1
, 57 kDa RNA-binding protein PPTB-1
, RNA-binding protein
, heterogeneous nuclear ribonucleoprotein I
, heterogeneous nuclear ribonucleoprotein polypeptide I
, hnRNP I
, polypyrimidine tract binding protein (heterogeneous nuclear ribonucleoprotein I)
, pyrimidine binding protein 1
, pyrimidine binding protein 2
, brom bones